Gopod format

Manufactured by Megazyme

Sourced in Ireland

The GOPOD Format is a laboratory equipment product used for the measurement and quantification of glucose, sucrose, and fructose. It provides a standardized method for the analysis of these analytes in various sample types.

Automatically generated - may contain errors

Lab products found in correlation

Gastric mucin, by Merck Group (1 mentions) Amyloglucosidase, by Solarbio (1 mentions) Pancreatin, by Solarbio (1 mentions) α amylase, by Merck Group (1 mentions) Pepsin, by Solarbio (1 mentions) Phosphate buffered saline (pbs), by Merck Group (1 mentions) Tannic acid, by Merck Group (1 mentions) Alliance hplc, by Waters Corporation (1 mentions) Microq tof mass spectrometer, by Waters Corporation (1 mentions) D xylose assay kit, by Megazyme (1 mentions)

5 protocols using gopod format

In vitro gastrointestinal digestion of starch

Check if the same lab product or an alternative is used in the 5 most similar protocols

Artificial rat saliva and gastric juice were prepared following the method of Chen et al. [10 (link)] and Wu et al. [14 (link)]. Artificial pancreatic juice and bile juice were prepared according to Wu et al. [15 (link)]. Glucose concentration was determined with a D-glucose assay kit (GOPOD-Format) (Megazyme International Ireland Ltd., Wicklow, Ireland). Gastric mucin and α-amylase were obtained from Sigma (Sigma-Aldrich, Saint Louis, MO, USA). Amyloglucosidase, pancreatin, and pepsin were obtained from Solarbio (Shanghai Solarbio Bioscience & Technology Co. Ltd., Shanghai, China). All other chemical reagents were obtained from Sinopharm Chemical Reagent Co. Ltd. (Beijing, China).
The DIVRSD-II model was applied to digestion of HPH-treated starch [15 (link)]. Starch samples (200 mg, dry basis) were dispersed in 2.0 mL of water and cooked for 15 min until gelatinized. Then 2.0 mL of artificial saliva (37 °C) was added to mimic oral digestion [16 (link)]. The food samples were digested in the DIVRSD-II model in batches as reported by Wu et al. [15 (link)] for 0, 10, 20, 30, 40, 50, 60, 90, 120 and 180 min.

Guo Z., Zhao B., Chen L, & Zheng B. (2019). Physicochemical Properties and Digestion of Lotus Seed Starch under High-Pressure Homogenization. Nutrients, 11(2), 371.

+ Open protocol

+ Expand

Reusability of Immobilized Enzymes

Check if the same lab product or an alternative is used in the 5 most similar protocols

To assess the possibility of recycling the immobilized enzyme preparations for conversion, immobilized β-gal LacLM L. reuteri L103 was added to sodium phosphate buffer (50 mM, pH 6.5) containing 600 mM lactose and maintained at 30 °C and 600 rpm agitation for the conversion of lactose. Every 24 h, the chitin beads carrying the enzyme were filtered off, rinsed with buffer, and reused in another batch conversion experiment under identical conditions. The filtrates from every conversion cycle were collected to determine the glucose concentration by using a commercial d-glucose assay kit (GOPOD Format, Megazyme, Wicklow, Ireland). The glucose concentration in the filtrate from the first conversion was taken as 100% of converting ability of the immobilized enzyme preparation.
Immobilized LacZ from L. bulgaricus DSM 20081 was also tested for its reusability but using the substrate oNPG. After 5 min of incubation with o-nitrophenyl-β-d-galactopyranoside (oNPG) at 30 °C, chitin beads carrying LacZ were separated from the liquid phase and reused in the next conversion experiments. The concentration of oNPG in the liquid phases after the conversion was measured with a spectrophotometer at 420 nm and used to calculate the residual converting ability of enzyme in each repeating conversion.

Pham M.L., Leister T., Nguyen H.A., Do B.C., Pham A.T., Haltrich D., Yamabhai M., Nguyen T.H, & Nguyen T.T. (2017). Immobilization of β-Galactosidases from Lactobacillus on Chitin Using a Chitin-Binding Domain. Journal of agricultural and food chemistry, 65(14), 2965-2976.

+ Open protocol

+ Expand

Enzymatic Hydrolysis of Maize Starch

Check if the same lab product or an alternative is used in the 5 most similar protocols

Tannic acid, AA (EC 3.2.1.1) from porcine pancreas, AMG (EC 3.2.1.3,) from Aspergillus niger, phosphate-buffered saline (PBS) tablets, and p-hydroxybenzoic acid hydrazide (PAHBAH) were purchased from Sigma-Aldrich Co. (St. Louis, US). Normal maize starch was obtained from Yuanye Biotech. Co. (Shanghai, China). A _D-glucose assay kit (GOPOD-FORMAT) was obtained from Megazyme® (Megazyme E-AMGDF). Other chemicals were of analytical grade.

Li S., Wu W., Li J., Zhu S., Yang X, & Sun L. (2022). α-Amylase Changed the Catalytic Behaviors of Amyloglucosidase Regarding Starch Digestion Both in the Absence and Presence of Tannic Acid. Frontiers in Nutrition, 9, 817039.

+ Open protocol

+ Expand

Comprehensive Carbohydrate and Protein Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total carbohydrate content was determined by Bernfeld ([1955 ]) method using a xylose-based calibration curve. Xylose was determined by D-xylose assay kit (Megazyme), specifically designed to measure this sugar in samples containing up to 5 mg of glucose in the final assay reaction without any interference. Glucose was assayed enzymatically by GOPOD-FORMAT, Megazyme. Protein concentration was determined by the method of Bradford ([1976 (link)]) using bovine serum albumin as the standard. Thermomyces lanuginosus xylanase, (X2753 2500 U/g) was obtained from Sigma. Thermotoga maritima endo-1,4-β-xylanase, 22 U/mg of protein (wheat arabinoxylan at pH 5.0 and 40°C) was obtained from Megazyme.
¹H NMR spectra were recorded at 600.13 MHz on a Bruker DRX-600 spectrometer, equipped with a TCI Cryo Probe TM, fitted with a gradient along the Z-axis. Spectra in D₂O were referenced to internal sodium 3-(trimethyl-silyl)-(2,2,3,3-2H4) propionate (Aldrich, Milwaukee, WI). ¹³C NMR, JMOD-¹H and COSY, TOCSY, HSQC, HSQC-EDITED, HMBC (³ J: 7 and 10 Hz), NOESY (mixing time at 100, 200, 300 msec) experiments were used for structural determination.
Mass spectra were acquired on a microQ-Tof mass spectrometer coupled with an Alliance HPLC (Waters, Milford, MA) equipped with an ESI source.

Lama L., Tramice A., Finore I., Anzelmo G., Calandrelli V., Pagnotta E., Tommonaro G., Poli A., Di Donato P., Nicolaus B., Fagnano M., Mori M., Impagliazzo A, & Trincone A. (2014). Degradative actions of microbial xylanolytic activities on hemicelluloses from rhizome of Arundo donax. AMB Express, 4, 55.

+ Open protocol

+ Expand

Measurement of β-Galactosidase Activity

Check if the same lab product or an alternative is used in the 5 most similar protocols

The b-galactosidase activity towards lactose under relevant GOS production conditions was measured using an oxidase/peroxidase method (GOPOD Format, Megazyme, Ireland). One unit (U) of (total) activity was defined as the enzyme amount required to release 1 lmol Glc per min. For rBgaD-D, 50% lactose (w/w) in 0.1 M sodium phosphate buffer (pH 6.0) was used as substrate (Park & Oh, 2010) (link), incubated at 60 °C for 5 min. For Lactozyme 2600L, 30% lactose (w/w) in 0.1 M sodium phosphate buffer (pH 7.0) was used and the mixture was incubated at 40 °C for 5 min (Zhou & Chen, 2001) (link). For the b-galactosidase from A. oryzae, 30% lactose (w/w) in 0.1 M sodium acetate buffer (pH 4.5) was used and incubation was carried out at 45 °C for 5 min (Vera et al., 2011) (link). Different lactose concentrations were used reflecting the solubility of lactose at the respective enzyme optimum temperature. After 5 min, the reactions were stopped immediately by adding 1.5 M NaOH, followed by neutralization with 1.5 M HCl. The amount of released Glc was determined in the GOPOD assay by measuring the absorbance at 510 nm.

Yin H., Bultema J.B., Dijkhuizen L, & van Leeuwen S.S. (2017). Reaction kinetics and galactooligosaccharide product profiles of the β-galactosidases from Bacillus circulans, Kluyveromyces lactis and Aspergillus oryzae. Food chemistry, 225.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!